Folia Microbiologica

, Volume 48, Issue 2, pp 168–172 | Cite as

Purification and partial characterization of α-l-arabinofuranosidase produced byThermomonospora fusca

  • M. Tuncer
  • A. S. Ball


Thermomonospora fusca produced a relatively high level of α-l-arabinofuranosidase when growing on oat spelt xylan as the main carbon and energy source. The enzyme exhibited maximum relative activity (0.136 U/g protein) at pH 9.0 with 54 and 55% activity remaining at pH of 4.5 and 11.0, respectively. The apparentKm value for the crude α-l-arabinofuranosidase preparation was 180 µmol/L 4-nitrophenyl α-l-arabinofuranoside; thevlim value was the release of 40 µmol/L 4-nitrophenol per min. Enzyme activity was eluted as a single peak (HPLC gel filtration chromatography) corresponding to molar mass of ≈92 kDa. Native electrophoresis of crude cell lysate confirmed the presence of a single active intracellular α-l-arabinofuranosidase component. SDS-PAGE of this enzyme, developed as zymogram, did not demonstrate any activity; denaturing gel was stained and a protein band of relative molar mass of 46 kDa was revealed. Isoelectric focusing of a purified α-l-arabinofuranosidase yielded a single protein band for the corresponding activity zone with pI 7.9. The enzyme was purified approximately 21-fold the mean overall yield was about 16%.


Fusca Single Protein Band Lignocellulose Degradation Crude Cell Lysate Native Electrophoresis 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.



isoelectric focusing


4-nitrophenyl α-l-arabinofuranoside


polyacrylamide gel electrophoresis


sodium dodecyl sulfate


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© Institute of Microbiology, Academy of Sciences of the Czech Republic 2003

Authors and Affiliations

  1. 1.Biyoloji Bölümü, Fen-Edebiyat FakültesiMersin ÜniversitesiMersinTurkey
  2. 2.John Tabor Laboratories, Department of Biological SciencesUniversity of EssexColchesterUK

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